PXD040236 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2 |
Description | Post-translational modifications (PTMs) of histones have fundamental effects on chromatin structure and function. While the impact of PTMs on the function of core histones are increasingly well understood, this is much less the case for modifications of linker histone H1, which is at least in part due to a lack of proper tools. In this work, we establish the assembly of intact chromatosomes containing site-specifically ubiquitylated and acetylated linker histone H1.2 variants obtained by a combination of chemical biology approaches. We then use these complexes in a tailored affinity enrichment mass spectrometry workflow to identify and comprehensively characterize chromatosome-specific cellular interactomes and the impact of site-specific linker histone modifications on a proteome-wide scale. We validate and benchmark our approach by western-blotting and by confirming the involvement of chromatin-bound H1.2 in the recruitment of proteins involved in DNA double-strand break repair using an in vitro ligation assay. We relate our data to previous work and in particular compare it to data on modification-specific interaction partners of free H1. Taken together, our data supports the role of chromatin-bound H1 as a regulatory protein with distinct functions beyond DNA compaction and constitutes an important resource for future investigations of histone epigenetic modifications. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_06:13:40.899.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Philip Saumer |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-02-17 06:55:00 | ID requested | |
1 | 2023-11-02 10:39:12 | announced | |
2 | 2024-01-15 07:56:11 | announced | 2024-01-15: Updated project metadata. |
⏵ 3 | 2024-10-22 06:13:44 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1093/nar/gkad1113; |
Saumer P, Scheffner M, Marx A, Stengel F, Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2. Nucleic Acids Res, 52(1):101-113(2024) [pubmed] |
Keyword List
submitter keyword: affinity enrichment,: Proteomics, Post-translational modification, chromatosome, chemical biology, linker histone |
Contact List
Florian Stengel |
contact affiliation | Laboratory of Biochemistry and Mass Spectrometry, Department of Biology, University of Konstanz |
contact email | florian.stengel@uni-konstanz.de |
lab head | |
Philip Saumer |
contact affiliation | University of Konstanz |
contact email | philip.saumer@uni-konstanz.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/11/PXD040236 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD040236
- Label: PRIDE project
- Name: Interactome of intact chromatosome variants with site-specifically ubiquitylated and acetylated linker histone H1.2